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The structure of a polygamous repressor reveals how phage-inducible chromosomal islands spread in nature

DOI: 10.1038/s41467-019-11504-2 DOI Help

Authors: J. Rafael Ciges-tomas (Instituto de Biomedicina de Valencia (IBV-CSIC); CIBER de Enfermedades Raras (CIBERER)) , Christian Alite (Instituto de Biomedicina de Valencia (IBV-CSIC); CIBER de Enfermedades Raras (CIBERER)) , Suzanne Humphrey (University of Glasgow) , Jorge Donderis (Instituto de Biomedicina de Valencia, Consejo Superior de Investigaciones Científicas (IBV-CSIC)) , Janine Bowring (University of Glasgow) , Xavier Salvatella (ICREA and Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology) , José R. Penadés (University of Glasgow) , Alberto Marina (nstituto de Biomedicina de Valencia (IBV-CSIC); CIBER de Enfermedades Raras (CIBERER))
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 10

State: Published (Approved)
Published: August 2019
Diamond Proposal Number(s): 14739 , 16258

Open Access Open Access

Abstract: Stl is a master repressor encoded by Staphylococcus aureus pathogenicity islands (SaPIs) that maintains integration of these elements in the bacterial chromosome. After infection or induction of a resident helper phage, SaPIs are de-repressed by specific interactions of phage proteins with Stl. SaPIs have evolved a fascinating mechanism to ensure their promiscuous transfer by targeting structurally unrelated proteins performing identically conserved functions for the phage. Here we decipher the molecular mechanism of this elegant strategy by determining the structure of SaPIbov1 Stl alone and in complex with two structurally unrelated dUTPases from different S. aureus phages. Remarkably, SaPIbov1 Stl has evolved different domains implicated in DNA and partner recognition specificity. This work presents the solved structure of a SaPI repressor protein and the discovery of a modular repressor that acquires multispecificity through domain recruiting. Our results establish the mechanism that allows widespread dissemination of SaPIs in nature.

Journal Keywords: Coevolution; Phage biology; X-ray crystallography

Subject Areas: Biology and Bio-materials


Instruments: I03-Macromolecular Crystallography , I04-Macromolecular Crystallography

Other Facilities: ALBA

Documents:
s41467-019-11504-2.pdf